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Archives of Virology

Erschienen in:

01.07.2009 | Original Article

MDV-1 VP22: a transporter that can selectively deliver proteins into cells

verfasst von: Chenfei Zhang, Aijian Qin, Hongjun Chen, Xufang Deng, Yuwen Su, Kun Qian

Erschienen in: Archives of Virology | Ausgabe 7/2009

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Abstract

The tegument protein VP22 of Marek’s disease virus (MDV) was previously shown to be able to travel between cells. To further characterize the transport property of VP22 and assess whether it can be used for protein delivery, we investigated the subcellular localization of VP22 fused to five heterologous proteins, including green fluorescent protein, nucleoprotein of avian influenza virus, bovine IFN-γ, F protein of Newcastle disease virus and VP2 protein of infectious bursa disease virus. The transport of these fusion proteins in monolayer cells was assayed by immunofluorescence assay. The results showed that all except VP2 could be delivered by VP22 of MDV serotype 1 (MDV-1), at different efficiencies. After being transported to surrounding cells, VP22 fused to avian influenza nucleoprotein, bovine IFN-γ, or to F was localized in the nucleus. Our data suggest that VP22 of MDV-1 can be used as transport tool in protein delivery and that the original localization of cargo proteins may be changed after transport by MDV-1 VP22. Finally, infectious bursa disease VP2 protein could not be transported by MDV-1 VP22.

Anton LC, Schubert U, Bacik I, Princiotta MF, Wearsch PA, Gibbs J, Day PM, Realini C, Rechsteiner MC, Bennink JR, Yewdell JW (1999) Intracellular localization of proteasomal degradation of a viral antigen. J Cell Biol 146:113–124PubMed

Biswas SK, Boutz PL, Nayak DP (1998) Influenza virus nucleoprotein interacts with influenza virus polymerase proteins. J Virol 72:5493–5501PubMed

Bullido R, Gomez-Puertas P, Albo C, Portela A (2000) Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein. J Gen Virol 81:135–142PubMed

Cao L, Si J, Wang W, Zhao X, Yuan X, Zhu H, Wu X, Zhu J, Shen G (2006) Intracellular localization and sustained prodrug cell killing activity of TAT-HSVTK fusion protein in hepatocelullar carcinoma cells. Mol Cells 21:104–111PubMed

Cashman SM, Morris DJ, Kumar-Singh R (2003) Evidence of protein transduction but not intercellular transport by proteins fused to HIV tat in retinal cell culture and in vivo. Mol Ther 8:130–142PubMedCrossRef

Chauhan A, Turchan J, Pocernich C, Bruce-Keller A, Roth S, Butterfield DA, Major EO, Nath A (2003) Intracellular human immunodeficiency virus Tat expression in astrocytes promotes astrocyte survival but induces potent neurotoxicity at distant sites via axonal transport. J Biol Chem 278:13512–13519PubMedCrossRef

Chauhan A, Tikoo A, Kapur AK, Singh M (2007) The taming of the cell penetrating domain of the HIV Tat: myths and realities. J Control Release 117:148–162PubMedCrossRef

Chen H, Song C, Qin A, Zhang C (2007) Expression and intercellular trafficking of the VP22 protein of CVI988/Rispens vaccine strain of Marek’s disease virus. Sci China C Life Sci 50:75–79PubMedCrossRef

Chen H, Zhang C, Song C, Deng X, Qin A (2008) MDV-1 VP22 conjugated VP2 enhancing immune response against infectious bursal disease virus by DNA vaccination in mice. Sci China C Life Sci 51:981–986PubMedCrossRef

10.

Efthymiadis A, Briggs LJ, Jans DA (1998) The HIV-1 Tat nuclear localization sequence confers novel nuclear import properties. J Biol Chem 273:1623–1628PubMedCrossRef

11.

Frankel AD, Pabo CO (1988) Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55:1189–1193PubMedCrossRef

12.

Futami J, Kitazoe M, Maeda T, Nukui E, Sakaguchi M, Kosaka J, Miyazaki M, Kosaka M, Tada H, Seno M, Sasaki J, Huh NH, Namba M, Yamada H (2005) Intracellular delivery of proteins into mammalian living cells by polyethylenimine-cationization. J Biosci Bioeng 99:95–103PubMedCrossRef

13.

Green M, Loewenstein PM (1988) Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 55:1179–1188PubMedCrossRef

14.

Kohler G, Milstein C (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256:495–497PubMedCrossRef

15.

Kueltzo LA, Normand N, O’Hare P, Middaugh CR (2000) Conformational lability of herpesvirus protein VP22. J Biol Chem 275:33213–33221PubMedCrossRef

16.

Leifert JA, Harkins S, Whitton JL (2002) Full-length proteins attached to the HIV tat protein transduction domain are neither transduced between cells, nor exhibit enhanced immunogenicity. Gene Ther 9:1422–1428PubMedCrossRef

17.

Lundberg M, Johansson M (2001) Is VP22 nuclear homing an artifact? Nat Biotechnol 19:713–714PubMedCrossRef

18.

Lundberg M, Wikstrom S, Johansson M (2003) Cell surface adherence and endocytosis of protein transduction domains. Mol Ther 8:143–150PubMedCrossRef

19.

Morris MC, Depollier J, Mery J, Heitz F, Divita G (2001) A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat Biotechnol 19:1173–1176PubMedCrossRef

20.

Neumann G, Castrucci MR, Kawaoka Y (1997) Nuclear import and export of influenza virus nucleoprotein. J Virol 71:9690–9700PubMed

21.

O’Neill RE, Talon J, Palese P (1998) The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J 17:288–296PubMedCrossRef

22.

Rao SS, Gomez P, Mascola JR, Dang V, Krivulka GR, Yu F, Lord CI, Shen L, Bailer R, Nabel GJ, Letvin NL (2006) Comparative evaluation of three different intramuscular delivery methods for DNA immunization in a nonhuman primate animal model. Vaccine 24:367–373PubMedCrossRef

23.

Saha S, Yoshida S, Ohba K, Matsui K, Matsuda T, Takeshita F, Umeda K, Tamura Y, Okuda K, Klinman D, Xin KQ, Okuda K (2006) A fused gene of nucleoprotein (NP) and herpes simplex virus genes (VP22) induces highly protective immunity against different subtypes of influenza virus. Virology 354:48–57PubMedCrossRef

24.

Snyder EL, Dowdy SF (2001) Protein/peptide transduction domains: potential to deliver large DNA molecules into cells. Curr Opin Mol Ther 3:147–152PubMed

25.

Song CP, Chen HJ, Qin AJ, Zhang CF (2007) Preparation and immunological characterization of monoclonal antibodies against VP22 carboxyl terminus of Marek’s disease virus serotype 1. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 23:249–252PubMed

26.

Stauber RH, Pavlakis GN (1998) Intracellular trafficking and interactions of the HIV-1 Tat protein. Virology 252:126–136PubMedCrossRef

27.

Sugita T, Yoshikawa T, Mukai Y, Yamanada N, Imai S, Nagano K, Yoshida Y, Shibata H, Yoshioka Y, Nakagawa S, Kamada H, Tsunoda SI, Tsutsumi Y (2008) Comparative study on transduction and toxicity of protein transduction domains. Br J Pharmacol 153:1143–1152PubMedCrossRef

28.

Tasciotti E, Giacca M (2005) Fusion of the human immunodeficiency virus type 1 tat protein transduction domain to thymidine kinase increases bystander effect and induces enhanced tumor killing in vivo. Hum Gene Ther 16:1389–1403PubMedCrossRef

29.

Trollet C, Bloquel C, Scherman D, Bigey P (2006) Electrotransfer into skeletal muscle for protein expression. Curr Gene Ther 6:561–578PubMedCrossRef

30.

Ulmer JB, Deck RR, DeWitt CM, Friedman A, Donnelly JJ, Liu MA (1994) Protective immunity by intramuscular injection of low doses of influenza virus DNA vaccines. Vaccine 12:1541–1544PubMedCrossRef

31.

Workman P (2003) The opportunities and challenges of personalized genome-based molecular therapies for cancer: targets, technologies, and molecular chaperones. Cancer Chemother Pharmacol 52(Suppl 1):S45–S56PubMedCrossRef

32.

Zoonens M, Reshetnyak YK, Engelman DM (2008) Bilayer interactions of pHLIP, a peptide that can deliver drugs and target tumors. Biophys J 95:225–235PubMedCrossRef

Titel: MDV-1 VP22: a transporter that can selectively deliver proteins into cells
verfasst von: Chenfei Zhang
Aijian Qin
Hongjun Chen
Xufang Deng
Yuwen Su
Kun Qian
Publikationsdatum: 01.07.2009
Verlag: Springer Vienna
Erschienen in: Archives of Virology / Ausgabe 7/2009
Print ISSN: 0304-8608
Elektronische ISSN: 1432-8798
DOI: https://doi.org/10.1007/s00705-009-0404-y

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